2012
DOI: 10.1016/j.jcs.2011.12.002
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Gliadin and zein show similar and improved rheological behavior when mixed with high molecular weight glutenin

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Cited by 40 publications
(21 citation statements)
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“…The increase in water level showed a decline in dough consistency as well as stability. Fevzioglu et al (2012) observed that the more consistent doughs were made when water was less.…”
Section: Mixographic Propertiesmentioning
confidence: 95%
See 1 more Smart Citation
“…The increase in water level showed a decline in dough consistency as well as stability. Fevzioglu et al (2012) observed that the more consistent doughs were made when water was less.…”
Section: Mixographic Propertiesmentioning
confidence: 95%
“…This indicated the formation of weaker dough at high water level when compared with the dough made at lower water levels. Fevzioglu et al (2012) observed that the moduli of dough samples decreased with increase in water level. Chel-Guerrero et al (2015) reported that the lower tan d for corn dough made the tortilla preparation difficult.…”
Section: Dynamic Rheologymentioning
confidence: 96%
“…High‐molecular weight glutenin (HMWG) can contribute to the elasticity of wheat dough. Fevzioglu and others () demonstrated that zein proteins can behave in a similar manner to gliadin upon the addition of HMWG. To produce a stable viscoelastic structure, rheological methods, for example, large strain (uniaxial and biaxial) and small strain tests, were utilized to assess the effect of HMWG.…”
Section: New Approaches To Aid Processing and Enhance Nutritionmentioning
confidence: 99%
“…The maize endosperm proteins simply lack the additional elastic high molecular weight glutenin subunits (HMW-GS) function of wheat, and the addition of a minor amount of this or another similar protein would confer viscoelasticity to the mixture. Co-protein, namely HMW-GS or casein (as a non-wheat protein), stabilized the viscoelasticity of the hydrated, heated (to 35°C), and mixed maize zein, as well as held stable the β-sheet content after mixing (98). The β- sheet structures are made from extended β-strand polypeptide chains, with strands linked to their neighbors by hydrogen bond and, due to this extended backbone conformation, β-sheets resisted stretching.…”
Section: Gluten-free Floursmentioning
confidence: 99%